Evidence map›Paper›PMID 29046357›Full record

ArticleThe Journal of biological chemistry2017

Structural and thermodynamic analyses reveal critical features of glycopeptide recognition by the human PILRα immune cell receptor.

Atsushi Furukawa, Kosuke Kakita, Tomoki Yamada, Mikihiro Ishizuka, Jiro Sakamoto, Nanao Hatori, Naoyoshi Maeda, Fumina Ohsaka, Takashi Saitoh, Takao Nomura and 8 more

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.4field-weighted citation impact, top 36% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Mucin-Type O-GalNAc Glycosylation in Health and Disease.Advances in experimental medicine and biology · 2021
    Article
  5. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

18 authors at 4 institutions in 2 countries.

Atsushi FurukawaFrom the Laboratories of Biomolecular Science and.ORCID 0000-0003-1281-2252
Kosuke KakitaSynthetic and Industrial Chemistry, Faculty of Pharmaceutical Sciences and.
Tomoki YamadaCenter for Research and Education on Drug Discovery, Hokkaido University, Sapporo 060-0812, Japan and.
Mikihiro IshizukaFrom the Laboratories of Biomolecular Science and.
Jiro SakamotoFrom the Laboratories of Biomolecular Science and.
Nanao HatoriSynthetic and Industrial Chemistry, Faculty of Pharmaceutical Sciences and.
Naoyoshi MaedaCenter for Research and Education on Drug Discovery, Hokkaido University, Sapporo 060-0812, Japan and.
Fumina OhsakaCenter for Research and Education on Drug Discovery, Hokkaido University, Sapporo 060-0812, Japan and.
Takashi SaitohCenter for Research and Education on Drug Discovery, Hokkaido University, Sapporo 060-0812, Japan and.
Takao NomuraCenter for Research and Education on Drug Discovery, Hokkaido University, Sapporo 060-0812, Japan and.
Kimiko KurokiFrom the Laboratories of Biomolecular Science and.ORCID 0000-0001-9796-4217
Hisanori NambuSynthetic and Industrial Chemistry, Faculty of Pharmaceutical Sciences and.
Hisashi AraseWorld Premier International Immunology Frontier Research Center and.ORCID 0000-0002-1153-3166
Shigeki MatsunagaSynthetic and Industrial Chemistry, Faculty of Pharmaceutical Sciences and.
Masahiro AnadaSynthetic and Industrial Chemistry, Faculty of Pharmaceutical Sciences and.
Toyoyuki OseFrom the Laboratories of Biomolecular Science and.
Shunichi HashimotoSynthetic and Industrial Chemistry, Faculty of Pharmaceutical Sciences and.
Katsumi MaenakaFrom the Laboratories of Biomolecular Science and maenaka@pharm.hokudai.ac.jp.ORCID 0000-0002-5459-521X
Hokkaido University of Education · JPSynthetic Biologics (United States) · USApplied Science Laboratories (United States) · USOsaka International University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Before entering host cells, herpes simplex virus-1 uses its envelope glycoprotein B to bind paired immunoglobulin-like type 2 receptor α (PILRα) on immune cells. PILRα belongs to the Siglec (sialic acid (SA)-binding immunoglobulin-like lectin)-like family, members of which bind SA. PILRα is the only Siglec member to recognize not only the sialylated

Indexed as

Models, MolecularAcetylgalactosamineBinding SitesCalorimetryCrystallography, X-RayEscherichia coliHumansKineticsLigandsMembrane GlycoproteinsPeptide FragmentsPolysaccharidesProtein ConformationProtein Interaction Domains and MotifsReceptors, ImmunologicRecombinant ProteinsAcetylgalactosamineglycoprotein B, SimplexvirusLigandsMembrane GlycoproteinsPeptide FragmentsPILRA protein, humanPolysaccharidesReceptors, ImmunologicRecombinant ProteinsViral Envelope Proteinscell surface receptorimmunologyisothermal titration calorimetry (ITC)protein chemistryprotein structureX-ray crystallography

Identifiers

PMID29046357
PMCPMC5743085
OpenAlexW2766929302

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.